BIO 3153 Study Guide - Final Guide: Membrane Protein, Cell Membrane, Cytosol

1. The histones that form the core of the nucleosome get into the nucleus by which of the following?

a) Passive diffusion through nuclear pores

b) Selective and facilitated active transport through nuclear pores

c) Ribosomes located in the nucleus synthetize histones in the nucleus

d) Histones are made at the ER membrane and then diffuse to the nucleus

2. Membrane proteins that belong to the golgi, lysosome, or plasma membrane first pass through which organelle before reaching their final subcellular destination?

a) The golgi apparatus

b) The smooth ER

c) The nucleus

d) The ER membrane

e) The ER lumen

3. Where in the cell would a ribosomal protein be located if it has had its nuclear export signal inactivated (non-functional or non-existent).

a) The protein would be found in the ER lumen

b) The protein would remain in the nucleus

c) The protein would be secreted

d) The protein would remain in the cytoplasm

e) The protein would be in the ER membrane

4. Where would be the final destination of a protein if it contained a NLS anywhere in the protein sequence (and which is exposed to the cytoplasm after protein folding) but also contained an ER signal sequence at the carboxy terminus?

a) The ER lumen

b) The nucleus

c) The cytoplasm

d) The inner nuclear membrane

e) The ER membrane

5. The sequence K-D-E-L serves as a retention/retrieval signal for ER proteins.

a) True

b) False

6. The following are true for both cell membrane proteins and secretory proteins EXCEPT?

a) Precursors of the mature proteins contain signal sequence.

b) Both types of proteins contain stop-transfer sequences

c) Both types of proteins enter the ER while being synthetized

d) Both types of proteins pas through the golgi apparatus

e) Both are carried by clatherin-coated vesicles

7. If you isolate a regulated secreted protein from a secretory/storage vesicle and inject it into the cytosol, is will?

a) Be secreted through channels in the plasma membrane

b) Be taken up into secretory vesicle and secreted

c) Remain in the cytosol until it is degraded

d) Be taken up into the rough ER and follow the secretory pathway

1. Which cytosolic factor is most likely to associate with the signal sequence of a protein that is targeted co-translationally to the ER?

A chaperone of the Hsp70 family

The translocation channel

The ribosome

Signal recognition particle (SRP)

Signal peptidase

2. What is the most likely fate of a protein with an N-terminal hydrophobic sorting signal and an additional internal hydrophobic domain of 22 amino acids?

The protein stays in the cytosol

The protein is transported to mitochondria

Because the protein has an N-terminal sorting signal, the protein is translocated all the way into the ER lumen

The hydrophobic domain is recognized as a transmembrane domain once it is in the translocation channel and released sideways into the membrane

The hydrophobic domain is cleaved off by signal peptidase

3. Which of the following statements best describes N-glycosylation? N-glycosylation refers to........

the addition of a pre-formed sugar tree to a serine or threonine present in the cytosolic domain of a protein

the addition of a pre-formed sugar tree to a phospholipid to make a glycolipid

the addition of individual sugars to selected amino acids on a protein

the addition of a pre-formed sugar tree to an asparagine residue found within the consensus sequence Asn-X-Ser/Thr in an ER lumenal domain of a protein

the addition of a pre-formed sugar tree to an asparagine residue found within the consensus sequence Asn-X-Ser/Thr in a cytosolic domain of a protein

4. What is the most likely fate of a protein in which a mutation has led to misfolding in the ER?

It is sequestered by the proteasome in the cytosol

It is first tagged with ubiquitin in the ER and then degraded by the proteasome in the cytosol

It is first moved out of the ER, tagged with ubiquitin in the cytosol and then degraded by the proteasome in the cytosol

It associates with many chaperones in the ER, which guarantee its correct folding

Its misfolded state is recognized by chaperones in the ER, which will induce the protein's degradation by the proteasome in the ER.